Takai Yoshimi, Irie Kenji, Shimizu Kazuya, Sakisaka Toshiaki, Ikeda Wataru
Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan.
Cancer Sci. 2003 Aug;94(8):655-67. doi: 10.1111/j.1349-7006.2003.tb01499.x.
Nectins are a family of Ca(2+)-independent immunoglobulin-like cell-cell adhesion molecules consisting of four members, which homophilically and heterophilically trans-interact and cause cell-cell adhesion. Nectin-based cell-cell adhesion is involved in the formation of cadherin-based adherens junctions in epithelial cells and fibroblasts. The nectin-based cell-cell adhesion induces activation of Cdc42 and Rac small G proteins, which eventually regulate the formation of adherens junctions through reorganization of the actin cytoskeleton, gene expression through activation of a mitogen-activated protein kinase cascade, and cell polarization through cell polarity proteins. Five nectin-like molecules (necls), which have domain structures similar to those of nectins, have recently been identified and appear to play different roles from those of nectins. One of them, named necl-5, which does not homophilically trans-interact, but heterophilically trans-interacts with nectin-3, regulates cell migration and adhesion. In this article, the roles and modes of action of nectins and necls in cell adhesion, migration, and polarization are reviewed.
NECTIN 是一类不依赖 Ca(2+) 的免疫球蛋白样细胞间黏附分子家族,由四个成员组成,它们通过同源和异源反式相互作用导致细胞间黏附。基于NECTIN的细胞间黏附参与上皮细胞和成纤维细胞中基于钙黏蛋白的黏附连接的形成。基于NECTIN的细胞间黏附诱导Cdc42和Rac小G蛋白的激活,最终通过肌动蛋白细胞骨架的重组来调节黏附连接的形成,通过丝裂原活化蛋白激酶级联反应的激活来调节基因表达,并通过细胞极性蛋白来调节细胞极化。最近已鉴定出五个具有与NECTIN相似结构域结构的NECTIN样分子(necls),它们似乎发挥着与NECTIN不同的作用。其中一个名为necl-5,它不进行同源反式相互作用,而是与NECTIN-3进行异源反式相互作用,调节细胞迁移和黏附。本文综述了NECTIN和necls在细胞黏附、迁移和极化中的作用及作用方式。